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Understanding the role of the merlin interacting protein magicin as part of the mammalian Mediator complex
Author(s) -
Beyer Kim S,
Lee MingFen,
Gusella James F,
Näär Anders M,
Ramesh Vijaya
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a79-c
Subject(s) - mediator , rna polymerase ii , multiprotein complex , microbiology and biotechnology , nuclear localization sequence , biology , small interfering rna , nls , gene , transcription factor ii d , genetics , transfection , promoter , gene expression
The objective of this study is to understand the functions of magicin ( m erlin a nd G rb2 i nteracting c ytoskeletal prote in ), a protein that we have identified and characterized as a novel binding partner of merlin, the product of the NF2 tumor suppressor gene. A recent study independently identified magicin (Med28) as part of the mammalian Mediator complex. The Mediator is a multiprotein co‐activator that is required for transcriptional activation of RNA polymerase II transcribed genes by DNA binding transcription factors. Magicin is not only present in the cytoskeleton but also in the nucleus. Magicin does not contain a nuclear localization signal (NLS) but yeast‐two‐hybrid experiments identified importin α as binding partner for magicin, providing a possible mechanism for nuclear import. We have confirmed the association of magicin with the Mediator subunits Med6 and Med25 (ARC92). In order to get further insight into the role of magicin in transcriptional regulation, we performed expression profiling experiments comparing NIH3T3 cells transfected with siRNAs for magicin or control siRNAs. These experiments revealed several candidate genes which were confirmed by qRT‐PCR. We are currently investigating the role of magicin in the regulation of these genes using reporter assays. This work was supported by Department of Defense Grant DAMD17‐02‐0647 and by a research fellowship of the Deutsche Forschungsgemeinschaft (DFG) to K.S.B.